Sediment-related growth limitation of Elodea nuttallii as indicated by a fertilization experiment

1. A fertilization experiment was performed to identify the limiting nutrient for the growth of submerged vegetation in ditches of a peat-grassland system in the Netherlands, in which restoration measures involved ceasing fertilization, exporting nutrients by removal of above-ground plant mass and large-scale introduction of calcium-rich, nutrient-poor artesian water.
2. Growth of Elodea was significantly enhanced by enrichment with nitrogen alone, and by fertilization with nitrogen in combination with phosphorus, and by nitrogen in combination with phosphorus and potassium.
3. Plant tissue nutrient concentrations increased significantly, for nitrogen by enrichment with nitrogen alone, and with nitrogen in combination with phosphorus and potassium; for phosphorus by enrichment with phosphorus alone and with phosphorus in combination with nitrogen and potassium; tissue concentrations of potassium were not enhanced by any treatment.
4. The elemental ratios of treated plants indicated that nitrogen, rather than phosphorus, was limiting in all treatments, except in those involving nitrogen and NK enrichment (when phosphorus was limiting).
5. The efficiency with which plants used nutrients declined with increased supply of nitrogen and phosphorus, but was unchanged when potassium was increased. Efficiencies were similar to those of other aquatic macrophytes.     

Tetracyclines modulate cytosolic Ca2+ responses in the osteoclast associated with “Ca2+ receptor” activation

We report the effects of tetracycline analogues on cytosolic Ca²⁺ transients resulting from application of ionic nickel (Ni²⁺), a potent surrogate agonist of the osteoclast Ca²⁺ receptor. Preincubation with minocycline (1 mg/l) or a chemically modified tetracycline, 4-dedimethyl-aminotetracycline (CMT-1) (1 or 10 mg/l), resulted in a significant attenuation of the magnitude of the cytosolic [Ca²⁺] response to an application of 5 mM-[Ni²⁺]. Preincubation with doxycycline (1 or 10 mg/l) failed to produce similar results. In addition, application of minocycline alone (0.1–100 mg/l) resulted in a 3.5-fold elevation of cytosolic [Ca²⁺]. The results suggest a novel action of tetracyclines on the osteoclast Ca²⁺ receptor.     

Sediment-related growth limitation of Elodea nuttallii as indicated by a fertilization experiment

1. A fertilization experiment was performed to identify the limiting nutrient for the growth of submerged vegetation in ditches of a peat-grassland system in the Netherlands, in which restoration measures involved ceasing fertilization, exporting nutrients by removal of above-ground plant mass and large-scale introduction of calcium-rich, nutrient-poor artesian water.
2. Growth of Elodea was significantly enhanced by enrichment with nitrogen alone, and by fertilization with nitrogen in combination with phosphorus, and by nitrogen in combination with phosphorus and potassium.
3. Plant tissue nutrient concentrations increased significantly, for nitrogen by enrichment with nitrogen alone, and with nitrogen in combination with phosphorus and potassium; for phosphorus by enrichment with phosphorus alone and with phosphorus in combination with nitrogen and potassium; tissue concentrations of potassium were not enhanced by any treatment.
4. The elemental ratios of treated plants indicated that nitrogen, rather than phosphorus, was limiting in all treatments, except in those involving nitrogen and NK enrichment (when phosphorus was limiting).
5. The efficiency with which plants used nutrients declined with increased supply of nitrogen and phosphorus, but was unchanged when potassium was increased. Efficiencies were similar to those of other aquatic macrophytes.     

A small camel-milk protein rich in cysteine/half-cystine

A small protein (M_r about 14 000) rich in cysteine/half-cystine has been isolated from camel milk by exclusion chromatography and reverse-phase high-performance liquid chromatography. The N-terminal amino acid sequence shows a region with several positional identities with and -caseins, which however lack cysteine residues; postions 16–20 are identical and involve the serine residues that have been found to be phosphorylated in -caseins.     

Characterization of phospholipase A2 from the venom of Horned viper (Cerastes cerastes)

Phospholipase A2 has been purified from the venom of Horned viper (Cerastes cerastes) by gel permeation chromatography followed by reverse-phase HPLC. The primary structure was established by sequence analysis of the intact protein and its enzymic peptides. The structure has 120 residues, properties like other group IIB phospholipases, but only 45-55% identity with the enzyme from other viperid species, and large variations even within the species (26% residue differences at known positions in another form).     

Purification and characterization of a Kunitz-type trypsin inhibitor from Leaf-nosed viper venom.

A Kunitz-type trypsin inhibitor was purified from Leaf-nosed viper venom and the primary structure determined by peptide analysis. In relation to other trypsin inhibitors, the protein has an extended C-terminal segment and a distinct pattern of residue alterations at the functionally important contact sites with proteases.     

Goat erythrocyte calmodulin is not abnormal

Calmodulin was purified from goat erythrocyte hemolysate using heat treatment and Sephadex G-100 gel filtration chromatography. The molecular weight and Stokes, radius of the purified calmodulin was determined. The goat erythrocyte calmodulin stimulated (Ca(2+)-Mg2+)-ATPase but not (Mg2+)-ATPase and (Na(+)-K(+)-Mg2+)-ATPase. The (Ca(2+)-Mg2+)-ATPase of the erythrocyte membrane derived from human, rat, rabbit and pig were significantly stimulated.     

Primary structure of hemoglobin β-chain fromColumba livia (gray wild pigeon)

Primary structure of β-chain of pigeon is presented. It was determined by amino acid sequence analysis of intact β-chain and its peptides obtained by the enzymatic and chemical cleavage. Comparison of amino acid sequence of the chain with other available data shows β 14 Ile, β61 Lys, and β113 Ile as residues specific to pigeon. One important replacement at α₁β₁ contact is β55 Met→Ser.     

Ryanodine-affinity chromatography purifies 106 kD Ca release channels from skeletal and cardiac sarcoplasmic reticulum

A 106 kD protein was isolated from skeletal sarcoplasmic reticulum (SR) vesicles and shown to have the properties of SR Ca2+ release channels, including blockade by 5 nM ryanodine. In view of extensive reports that the ryanodine-receptor complex consists of four 565 kD junctional feet proteins (JFPs) and is the 'physiological' Ca2+ release channel, we prepared ryanodine-affinity columns to isolate its receptor site(s). Conditions known to maximize the association and dissociation of ryanodine to SR proteins were respectively used to link, then elute, the receptor(s) from ryanodine-affinity columns. The method purified a protein at about 100 kD from both rabbit skeletal and canine cardiac SR vesicles. The skeletal and cardiac proteins isolated by ryanodine-affinity chromatography were identified as the low molecular weight Ca2+ release channel through their antigenic reaction with an anti-106 kD monoclonal antibody. Upon reconstitution in planar bilayers, both skeletal and cardiac proteins revealed the presence of functional SR Ca2+ release channels. Surprisingly, ryanodine-affinity columns did not retain JFPs but purified 106 kD Ca2+ release channels which are a minor component (0.1-0.3%) of SR proteins.